AQP5 Membrane Protein Introduction

Introduction of AQP5

AQP5 is a member of the aquaporin family, and it is encoded by the AQP5 gene in humans. Along with AQP0, AQP2 and AQP6, AQP5 is mapped to chromosome 12q13. AQP5 is highly expressed in lung, lacrimal gland and especially in salivary gland, where it is regulated by acetylation of histone H423 and DNA methylation. It is documented that AQP5 is exclusively expressed on the apical membrane of AT1 cells in the rat lung and activation of AQP5 in AT1 cells is associated with increased Sp1 (a transcription factor) binding to the hypomethylated proximal AQP5 promote. Current researches on AQP5 are focused on its role in the salivary glands.

Function of AQP5 Membrane Protein

It is well known that AQP5 plays a role in the generation of saliva, tears and pulmonary secretions. In addition, it has been reported that AQP5 is highly expressed in numerous tumors and may be responsible for poor prognosis of multiple cancers, such as colorectal cancer. AQP5 silencing can significantly reduce the migration and invasion of colorectal cancer cells. Moreover, AQP5 silencing significantly inhibits the proliferation and promotes the apoptosis of A549 lung cancer cells in vitro and in vivo. The possible mechanism is that AQP5 decreases the activation of the extracellular signal-regulated kinase 1/2 signaling pathway in A549 cells, and leads to decreased levels of the downstream proteins c-Fos and phosphorylated cAMP response element-binding protein. Inhibition of AQP5 expression can effectively reduce the tumorigenicity of A549 cells in vivo.

Fig.1 Schematic diagram of mouse AQP5 transmembrane topology. (Kumari, 2012)

Application of AQP5 Membrane Protein in Literature

1. Castorena-Torres F., et al. Aquaporine-5 and epithelial sodium channel beta-subunit gene expression in gastric aspirates in human term newborns. Heliyon. 2018, 4: e00602. PubMed ID: 29862364
   
   

   In this article, the authors demonstrate that AQP5 and the β subunit of the epithelial sodium channel (β-ENaC) in the respiratory epithelium are associated with both transient tachypnea of the newborn and neonatal respiratory distress syndrome.

2. Bisw as R., et al. Low-level laser therapy with 850nm recovers salivary function via membrane redistribution of aquaporin 5 by reducing intracellular Ca(2+) overload and ER stress during hyperglycemia. Biochim Biophys Acta. 2018, 1862: 1770-1780. PubMed ID: 29751100
   
   

   This article suggests that high glucose will induce intracellular Ca²⁺ overload and ER stress, which may disrupt AQP5 functional expression. In addition, phosphorylation-dependent AQP5 membrane distribution is inhibited by high glucose and low-level laser therapy with 850 nm can increase AQP5 membrane distribution in hyperglycemia-induced hyposalivation and then improve salivary function.

3. Kumari S.S., et al. Aquaporin 5 promotes corneal wound healing. Exp Eye Res. 2018, 172: 152-158. PubMed ID: 29660329
   
   

   The article reveals that AQP5 improves cell migration, proliferation and wound healing, suggesting that AQP5 plays a significant role in corneal epithelial wound healing.

4. Li C., et al. Vasoactive Intestinal Peptide Protects Salivary Glands against Structural Injury and Secretory Dysfunction via IL-17A and AQP5 Regulation in a Model of Sjogren Syndrome. Neuroimmunomodulation. 2017, 24: 300-309. PubMed ID: 29617700
   
   

   The authors use a model of Sjögren syndrome (SS) to verify that vasoactive intestinal peptide (VIP) could not only modulate the immune response but also affect exocrine gland function, and that these therapeutic effects are associated with IL-17A and AQP5 regulation.

5. Zhang L., et al. Silencing of aquaporin 5 inhibits the growth of A549 lung cancer cells in vitro and in vivo. Int J Oncol. 2018, PubMed ID: 29568884
   
   

   The article indicates that AQP5 silencing will suppress the growth of A549 cells in vitro and in vivo, suggesting that it may serve as a therapeutic target in lung cancer.

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Reference

1. Kumari S S, et al. (2012). Spatial expression of aquaporin 5 in mammalian cornea and lens, and regulation of its localization by phosphokinase A. Mol Vis. 18: 957-967.

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